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• W2018941503 abstract "The catalytic properties and sensitivity to different inhibitors have been determined for the reverse transcriptase (RT) of group O human immunodeficiency virus type 1 (HIV-1). The RT-coding region was cloned from a new HIV-1 group O isolate from Spain, expressed inEscherichia coli,and purified by affinity chromatography. This new RT showed 79% amino acid sequence identity with the corresponding enzyme of group M subtype B strain BH10. The two enzymes showed very similar kinetics of RNA-dependent DNA polymerization using homopolymeric template-primers and RNase H specific activity. Inhibitor sensitivity to ddTTP and 3′-azido-2′,3′-dideoxythymidine triphosphate (AZTTP) was also similar for both enzymes. However, the two enzymes differed dramatically in their sensitivity to several inhibitors. While the RT of the BH10 isolate was sensitive to nevirapine and loviride (IC50ranged from 0.16 to 8.2 μM,depending on the substrates used), the enzyme of the Spanish HIV-1 group O isolate showed high-level resistance to those compounds (IC50> 200 μM). The amino acid sequence of the RT of group O HIV-1 contains three amino acids (Cys-181, Glu-179, and Gly-98), which are found in group M subtype B strains resistant to nonnucleoside RT inhibitors. The recombinant group O HIV-1 RT should be useful for studies aimed at discovering and designing drugs directed toward group O isolates of HIV-1." @default.
• W2018941503 created "2016-06-24" @default.
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• W2018941503 creator A5061687469 @default.
• W2018941503 date "1997-09-01" @default.
• W2018941503 modified "2023-10-03" @default.
• W2018941503 title "Characterization of the Reverse Transcriptase of a Human Immunodeficiency Virus Type 1 Group O Isolate" @default.
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• W2018941503 doi "https://doi.org/10.1006/viro.1997.8748" @default.
• W2018941503 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9325244" @default.
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